7TL8
1.95A resolution structure of independent phosphoglycerate mutase from S. aureus in complex with a macrocyclic peptide inhibitor (Sa-D3)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 19-ID |
Synchrotron site | NSLS-II |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-10-14 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97950 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 46.898, 74.172, 75.017 |
Unit cell angles | 90.00, 100.54, 90.00 |
Refinement procedure
Resolution | 46.110 - 1.950 |
R-factor | 0.1971 |
Rwork | 0.194 |
R-free | 0.25480 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4my4 |
Data reduction software | XDS |
Data scaling software | Aimless (0.7.7) |
Phasing software | PHASER |
Refinement software | PHENIX (1.20_4438) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 46.110 | 46.110 | 2.000 |
High resolution limit [Å] | 1.950 | 8.940 | 1.950 |
Rmerge | 0.083 | 0.024 | 0.816 |
Total number of observations | 123194 | 1363 | 8845 |
Number of reflections | 36494 | 404 | 2555 |
<I/σ(I)> | 10.3 | 35.5 | 1.6 |
Completeness [%] | 98.9 | 97.5 | 99.5 |
Redundancy | 3.4 | 3.4 | 3.5 |
CC(1/2) | 0.997 | 0.999 | 0.605 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291 | 25% (w/v) PEG 3350, 100 mM Bis-Tris, 200 mM ammonium acetate |